1NOS
MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN (DELTA 114), IMIDAZOLE COMPLEX
Summary for 1NOS
| Entry DOI | 10.2210/pdb1nos/pdb |
| Descriptor | INDUCIBLE NITRIC OXIDE SYNTHASE, PROTOPORPHYRIN IX CONTAINING FE, IMIDAZOLE, ... (4 entities in total) |
| Functional Keywords | nitric oxide, l-arginine monooxygenase, heme, imidazole, nos, no, oxidoreductase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 45893.84 |
| Authors | Crane, B.R.,Arvai, A.S.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A. (deposition date: 1997-09-28, release date: 1998-10-14, Last modification date: 2024-02-14) |
| Primary citation | Crane, B.R.,Arvai, A.S.,Gachhui, R.,Wu, C.,Ghosh, D.K.,Getzoff, E.D.,Stuehr, D.J.,Tainer, J.A. The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. Science, 278:425-431, 1997 Cited by PubMed Abstract: The nitric oxide synthase oxygenase domain (NOSox) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOSox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged beta sheet engenders a curved alpha-beta domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis. PubMed: 9334294DOI: 10.1126/science.278.5337.425 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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